{"doi":"10.1507/endocrj.k10e-236","title":"Characterization of Thr-354 in the human sodium/iodide symporter (NIS) by site-directed mutagenesis","abstract":null,"journal":"Endocrine Journal","year":2010,"id":613376,"datarank":0.10397207708399181,"base_score":0.6931471805599453,"endowment":0.6931471805599453,"self_citation_contribution":0.10397207708399181,"citation_network_contribution":0.0,"self_endowment_contribution":0.10397207708399181,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":1,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":1580189,"name":"Hirokazu Fujiwara","orcid":null,"position":1,"is_corresponding":false},{"id":188481,"name":"Susumu Tanaka","orcid":null,"position":2,"is_corresponding":false},{"id":1580192,"name":"Nobuyuki Amino","orcid":null,"position":3,"is_corresponding":false},{"id":1580187,"name":"Ke-ita Tatsumi","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Characterization of Thr-354 in the human sodium/iodide symporter (NIS) by site-directed mutagenesis","abstract":"Sodium/iodide symporter (NIS) is the key molecule concentrating iodide in the thyroid gland. The first-described human NIS (hNIS) mutation to cause a complete iodide transport defect was the T354P mutation. The Thr-354 lies in the midst of the putative ninth transmembrane segment which is well-conserved within the members of the SLC5A transporter family. Here we have investigated the molecular function of Thr-354 using site-directed mutagenesis and found that T354S and T354A mutations result in significantly decreased iodide transport activity, 50 % and 2 % of wild-type hNIS. Our findings indicate that whereas Thr-354 is indispensable for the complete NIS activity, the β-hydroxyl group accounts for half, and the α-helical structure alone contributes for one-fiftieth of wild-type hNIS activity.","is_dataset_classified":null,"base_score":0.0,"endowment":0.0,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"20834191","pmcid":null,"openalex_id":null,"authors":[],"funders":[],"total_grants":0,"fwci":null,"citation_percentile":null,"influential_citations":0,"citation_trend":[],"oa_status":null,"license":null,"oa_locations":[{"url":"http://www.jstage.jst.go.jp/article/endocrj/57/11/57_K10E-236/_pdf","host_type":"publisher"}],"fields_of_study":[],"mesh_terms":["Thyroid Gland","Cell Line","Humans","Symporters","Transfection","Mutagenesis, Site-Directed","Ion Transport","Point Mutation","Sodium-Iodide Symporters"],"keywords":[],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-02T07:53:08.361311Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}